Nkx6.1 (delta homeodomain)
- Known as:
- Nkx6.1 (delta homeodomain)
- Catalog number:
- 000718A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Nkx6.1 (delta homeodomain)
Related genes to: Nkx6.1 (delta homeodomain)
- Gene:
- AGPAT4 NIH gene
- Name:
- 1-acylglycerol-3-phosphate O-acyltransferase 4
- Previous symbol:
- -
- Synonyms:
- LPAAT-delta, dJ473J16.2
- Chromosome:
- 6q26
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-25
- Date modifiied:
- 2019-03-26
- Gene:
- CEBPD NIH gene
- Name:
- CCAAT enhancer binding protein delta
- Previous symbol:
- -
- Synonyms:
- CRP3, CELF, C/EBP-delta, NF-IL6-beta
- Chromosome:
- 8q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1992-06-24
- Date modifiied:
- 2018-02-23
- Gene:
- CSNK1D NIH gene
- Name:
- casein kinase 1 delta
- Previous symbol:
- -
- Synonyms:
- HCKID, CKID, CKIdelta
- Chromosome:
- 17q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-09-27
- Date modifiied:
- 2016-10-05
- Gene:
- DGKD NIH gene
- Name:
- diacylglycerol kinase delta
- Previous symbol:
- -
- Synonyms:
- KIAA0145, DGKdelta
- Chromosome:
- 2q37.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-02
- Date modifiied:
- 2016-10-05
- Gene:
- EIF2B4 NIH gene
- Name:
- eukaryotic translation initiation factor 2B subunit delta
- Previous symbol:
- -
- Synonyms:
- EIF2Bdelta, EIF-2B, DKFZP586J0119, EIF2B
- Chromosome:
- 2p23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-16
- Date modifiied:
- 2015-11-16
Related products to: Nkx6.1 (delta homeodomain)
(Asn5)-Delta-Sleep Inducing Peptide
(Asn5)-Delta-Sleep Inducing Peptide (rabbit), (Asn5)-DSIP (rabbit) 98% C35H49N11O14 CAS: 80064-67-1(Tyr1)-Delta-Sleep Inducing Peptide
(Tyr1)-Delta-Sleep Inducing Peptide (rabbit), (Tyr1)-DSIP (rabbit) 98% C33H47N9O16 CAS:(β-Asp5)-Delta-Sleep Inducing Peptide
(β-Asp5)-Delta-Sleep Inducing Peptide (rabbit), (β-Asp5)-DSIP (rabbit) 98% C35H48N10O15 CAS: 82602-88-81-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,AGPAT4,Bos taurus,Bovine,LPAAT-delta,Lysophosphatidic acid acyltra1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,AGPAT4,Homo sapiens,Human,LPAAT-delta,Lysophosphatidic acid acyltr1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,Agpat4,LPAAT-delta,Lysophosphatidic acid acyltransferase delta,Mou1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,Agpat4,LPAAT-delta,Lysophosphatidic acid acyltransferase delta,Rat1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Bos taurus,Bovine,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Phospholipase C-III,PLCD1,PLC-delta-1,PLC-III1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Homo sapiens,Human,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Phospholipase C-III,PLCD1,PLC-delta-1,PLC-III1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Mouse,Mus musculus,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Plcd,Plcd1,PLC-delta-11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Phospholipase C-III,Plcd1,PLC-delta-1,PLC-III,Rat,Rattus norvegicus1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3,Homo sapiens,Human,KIAA1964,Phosphoinositide phospholipase C-delta-3,Phospholipase C-delta-3,PLCD3,PLC-delta-31-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3,Kiaa1964,Mouse,Mus musculus,Phosphoinositide phospholipase C-delta-3,Phospholipase C-delta-3,Plcd3,PLC-delta-31-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4,Bos taurus,Bovine,Phosphoinositide phospholipase C-delta-4,Phospholipase C-delta-2,Phospholipase C-delta-4,PLC-85,PLCD2,PLCD4,PLC-delt1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4,Homo sapiens,hPLCD4,Human,Phosphoinositide phospholipase C-delta-4,Phospholipase C-delta-4,PLCD4,PLC-delta-4 Related articles to: Nkx6.1 (delta homeodomain)
- Impairment of pancreatic β-cell function is a primary etiology of type 2 diabetes mellitus (T2DM). The sulfated manno-glucuronan (GMn) was found to possess a backbone structure consisting of interspersing 1, 3-linked β-D-GlcpA residues and alternating 1, 2-linked α-D-Manp residues and 1, 4-linked β-D-GlcpA residues. Additionally, random sulfation occurs at the C6 position of the Man residues. GMn demonstrated no detectable cytotoxicity in MIN6 cells and attenuated palmitic acid (PA)-induced decreases in cell viability in a dose-dependent manner. Furthermore, GMn effectively reversed PA-impaired glucose-stimulated insulin secretion (GSIS) in a dose-dependent manner in both MIN6 cells and primary mouse islets. In vivo, GMn treatment significantly attenuated glycemic levels in high-fat diet/streptozotocin-induced type 2 diabetic mice, elevated β-cell insulin content, and decreased the proportions of α-, δ-, and pancreatic polypeptide (PP)-cells. Mechanistically, GMn significantly suppressed aldehyde dehydrogenase 1A3 (ALDH1A3)-mediated retinol metabolism and increased the expression of key β-cell identity/function markers, including PDX1, NKX6.1, MAFA, and NeuroD1, in pancreatic islets. Consistently, in vitro studies demonstrated that GMn counteracted PA-induced upregulation of ALDH1A3, while promoting the expression of the same set of β-cell transcription factors. Collectively, these findings indicate that GMn may enhance β-cell proliferation and reduces β-cell differentiation by downregulating ALDH1A3 expression. - Source: PubMed
Publication date: 2026/03/19
Zhang WenjingZhang FumingZou XiaotingWu NanHe SunyueLu LusiXu ChunyiXu WeiyingJin WeihuaZhou Jiaqiang - Tissue-engineered scaffolds are increasingly important for improving pancreatic islet transplantation, as conventional transplantation disrupts the pancreas's native vasculature and extracellular matrix, reducing islet viability and function. This underscores the need to develop a three-dimensional porous microencapsulation scaffold system that can replicate a supportive microenvironment, providing both mechanical stability and biological cues vital to preserving islet viability and function. This study investigated the potential of two freeze-dried and crosslinked gelatin-based scaffolds: Gelatin vinyl acetate copolymer (GeVAc) and gelatin with oxidized dextran dialdehyde (GELDEX), for supporting pancreatic islet culture. Their physicochemical properties, architecture, and wettability were analyzed using scanning electron microscopy and contact angle measurements. Both scaffolds exhibited hydrophilic, biocompatible, and structurally stable characteristics. Mouse pancreatic MIN6 cells were cultured on the scaffolds for 7 days to evaluate islet viability, extracellular matrix deposition and functionality through immunocytochemistry, glucose-stimulated insulin secretion (GSIS), and gene expression analysis. MIN6 cells adhered well to both scaffolds, forming dense monolayers and multicellular spheroids that resembled native islet clusters. GeVAc scaffolds showed significantly higher glucose sensitivity and glucose stimulation index (GSI) compared to GELDEX. While INS1 and PDX1 expression levels were comparable in both scaffolds, NKX6.1 expression was significantly higher in GeVAc. These findings indicate that scaffold architecture and surface characteristics play a crucial role in creating a supportive microenvironment for islet cluster formation, highlighting the potential of gelatin-based scaffolds as microencapsulation platforms for clinical islet transplantation in diabetes therapy. - Source: PubMed
Salim RukhiyaUnnikrishnan P SArya D AThomas Lynda V - - Source: PubMed
Publication date: 2026/04/14
Carty Senegal - Forkhead Box A2 (FOXA2) is a transcription factor essential for endodermal development and the formation and function of several metabolic organs, including the liver and pancreas. Within the pancreatic lineage, FOXA2 plays a crucial role in orchestrating islet development, maintaining β-cell identity, and regulating genes central to glucose sensing and insulin secretion. This review provides a comprehensive overview of FOXA2's dual role in both developmental and mature stages of pancreatic islets, highlighting its function as a gatekeeper of lineage specification and metabolic homeostasis. We describe FOXA2's dynamic expression patterns during embryogenesis, its regulatory interactions with other key transcription factors, such as PDX1 and NKX6.1, and its influence on chromatin accessibility during islet cell differentiation. Furthermore, we discuss the consequences of FOXA2 dysregulation, including impaired α- and β-cell maturation, loss of functional identity, and contributions to the pathogenesis of diabetes. Insights from mouse models, human stem cell-derived islets, and patient genetics underscore the clinical relevance of FOXA2 in monogenic and complex forms of diabetes. By integrating developmental biology, genomics, and disease modeling approaches, this review highlights FOXA2 as a central regulator connecting pancreatic organogenesis with long-term metabolic control. Understanding FOXA2's regulatory networks may open new avenues for therapeutic strategies aimed at restoring or preserving β-cell function in diabetes. - Source: PubMed
Publication date: 2025/12/09
Elsayed Ahmed KManzoor YusraAbdelalim Essam M - Islet transplantation, a validated therapy for type 1 diabetes, shows heterogeneous clinical outcomes. There is an unmet need for actionable biomarkers predicting islet graft potency before transplantation. We leveraged a comprehensive set of clinical data and islet samples to explore the relation between islet gene expression and clinical transplantation outcomes. We measured copy number with digital PCR in 114 clinical islet preparations and showed its linear correlation with islet graft function in a mouse bioassay, independently of islet mass, purity, and viability ( < 0.01). Analyzing the clinical outcomes of 34 patients who received two or three islet preparations, we showed the added value of total copy number to predict primary graft function, as compared with islet mass alone (Delong test, < 0.001). Using a multiple regression Cox model, adjusted for islet mass, purity, and viability, a high total copy number was independently correlated with 10-year survival of islet graft success [adjusted hazard ratio (HR) [95% CI]: 0.63 [0.43; 0.92], < 0.017] and insulin independence (HR [95% CI]: 0.70 [0.52; 93], < 0.01). This relation was confirmed in an independent cohort of nine patients receiving a single islet transplantation in other centers. Genetic silencing with anti- shRNA or pharmacological induction of NKX6.1 with silymarin in vitro indicated a causal link between gene expression and islet graft function. These results suggest that mRNA expression can predict islet graft function and may serve as an actionable biomarker of graft potency in β cell replacement. - Source: PubMed
Publication date: 2026/03/25
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